It is proposed to compare the glycoproteins derived from a mammary adenocarcinoma of the A-strain mouse, of the surface of the cells of two sublines, the non-strain specific TA3-Ha and the strain specific TA3-St. The isolation of the native glycoprotein, from which Glycoprotein fraction I is derived by proteolytic action, will be attempted after isolation of the plasma membranes from TA3-Ha cells. Further elucidation of the chemical structure of Glycoprotein fraction I will be sought, and the elucidation of the chemical structure and physical parameters of the native glycoprotein will also be attempted. These studies will be performed both on cells obtained in ascites form and in culture form. These studies will eventually be extended to other tumor cells. The biosynthesis of the carbohydrate moiety of Glycoprotein fraction I will be studied, as well as the metabolic pathway of galactose. Finally, various glycopeptides containing the asparagine-N-acetylglucosamine linkage, 2-acetamido-2-deoxy-beta-D-glycopyranosyl, alpha-D-mannopyranosyl residues, and other amino acid residues will be synthesized and tested as inhibitors of wheat-germ agglutinin and concanavalin A activity.